AMPL1_ORYSJ
ID AMPL1_ORYSJ Reviewed; 542 AA.
AC Q2QSB9; A0A0P0Y9T0; Q0INL2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Putative leucine aminopeptidase 1;
DE EC=3.4.11.1;
DE AltName: Full=Leucyl aminopeptidase 1;
DE Short=LAP 1;
DE AltName: Full=Proline aminopeptidase 1;
DE EC=3.4.11.5;
DE AltName: Full=Prolyl aminopeptidase 1;
GN OrderedLocusNames=Os12g0434400, LOC_Os12g24650;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
CC -!- FUNCTION: Presumably involved in the processing and regular turnover of
CC intracellular proteins. Catalyzes the removal of unsubstituted N-
CC terminal amino acids from various peptides (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa
CC is preferably Leu, but may be other amino acids including Pro
CC although not Arg or Lys, and Yaa may be Pro. Amino acid amides and
CC methyl esters are also readily hydrolyzed, but rates on arylamides
CC are exceedingly low.; EC=3.4.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P30184};
CC Note=Binds 2 Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:P30184};
CC -!- SUBUNIT: Homohexamer (dimer of homotrimers).
CC {ECO:0000250|UniProtKB:Q10712}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAT16960.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DP000011; ABA97701.2; -; Genomic_DNA.
DR EMBL; AP008218; BAF29703.1; -; Genomic_DNA.
DR EMBL; AP014968; BAT16960.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_015619002.1; XM_015763516.1.
DR AlphaFoldDB; Q2QSB9; -.
DR SMR; Q2QSB9; -.
DR STRING; 4530.OS12T0434400-00; -.
DR MEROPS; M17.A03; -.
DR PaxDb; Q2QSB9; -.
DR PRIDE; Q2QSB9; -.
DR GeneID; 4352123; -.
DR KEGG; osa:4352123; -.
DR eggNOG; KOG2597; Eukaryota.
DR HOGENOM; CLU_013734_5_1_1; -.
DR InParanoid; Q2QSB9; -.
DR OrthoDB; 701485at2759; -.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR Genevisible; Q2QSB9; OS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR InterPro; IPR008283; Peptidase_M17_N.
DR PANTHER; PTHR11963; PTHR11963; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Cytoplasm; Hydrolase; Manganese; Metal-binding; Protease;
KW Reference proteome.
FT CHAIN 1..542
FT /note="Putative leucine aminopeptidase 1"
FT /id="PRO_0000247502"
FT ACT_SITE 323
FT /evidence="ECO:0000255"
FT ACT_SITE 400
FT /evidence="ECO:0000255"
FT BINDING 294
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 299
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 299
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 336
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 396
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 398
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 398
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P30184"
SQ SEQUENCE 542 AA; 57142 MW; BD6D2ED97D7CEB69 CRC64;
MPNVVDPPQI SFAAKDMDLT EWEGDILAVL VTETDVSKAT SSSSRFTNAA AALAKLDGEL
GGLLSEASAE EEFAGRAGQS VALRLPTAPG LHGFKRVCLV GVGNNMPSSA AACRSTGETI
AAVAKSAQAR SAAVALASPP PGWVQGEDLR LNAAAAVASG VVLGLHEDRR YKSDSKKVHL
KQVDLIGFGS GQEMGRKLQY ANHVSSAVIF AKELVNSPAN VLTPAVLAEE ASNIASSYSD
VLTATILDEE KCRELKMGSY LAVAAASANP PHFIHLCYKP PGGNVKRKLA IVGKGLTFDR
FYLSLDNLLI VTKFVCIGGY NIKIGAVTTI ELMKKDMGGS AALFGAAKAL GQIKPPGVEV
HFISAACENM ISGTGMRPGD IVTASNGKTI EVDNTDAEGR LTLADALVYA CKLGVDKIID
LATLTGYCRI ALGPSIAGIL TPSDELDKEV AAAYEASGEK FWRLPLEESY WEQMKSSVAD
MLNTGSPLGG AITAGLFLKQ FVDEKVKWMH VDMAGPVWNY KKQEATGFGV STLVEWVLIN
SS
